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P48591

- RIR1_DROME

UniProt

P48591 - RIR1_DROME

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Protein
Ribonucleoside-diphosphate reductase large subunit
Gene
RnrL, CG5371
Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Provides the precursors necessary for DNA synthesis. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides.

Catalytic activityi

2'-deoxyribonucleoside diphosphate + thioredoxin disulfide + H2O = ribonucleoside diphosphate + thioredoxin.

Enzyme regulationi

Under complex allosteric control mediated by deoxynucleoside triphosphates and ATP binding to separate specificity and activation sites on the M1 subunit. The type of nucleotide bound at the specificity site determines substrate preference. It seems probable that ATP makes the enzyme reduce CDP and UDP, dGTP favors ADP reduction and dTTP favors GDP reduction. Stimulated by ATP and inhibited by dATP binding to the activity site By similarity.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei16 – 161Allosteric activator By similarity
Binding sitei64 – 641Allosteric activator By similarity
Binding sitei99 – 991Allosteric activator By similarity
Binding sitei213 – 2131Substrate By similarity
Sitei229 – 2291Important for hydrogen atom transfer By similarity
Sitei237 – 2371Allosteric effector binding, determines substrate specificity By similarity
Binding sitei258 – 2581Substrate; via amide nitrogen By similarity
Sitei267 – 2671Allosteric effector binding, determines substrate specificity By similarity
Active sitei438 – 4381Proton acceptor By similarity
Active sitei440 – 4401Cysteine radical intermediate By similarity
Active sitei442 – 4421Proton acceptor By similarity
Sitei455 – 4551Important for hydrogen atom transfer By similarity
Sitei748 – 7481Important for electron transfer By similarity
Sitei749 – 7491Important for electron transfer By similarity
Sitei807 – 8071Interacts with thioredoxin/glutaredoxin By similarity
Sitei810 – 8101Interacts with thioredoxin/glutaredoxin By similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor Source: UniProtKB
Complete GO annotation...

GO - Biological processi

  1. DNA replication Source: UniProtKB-UniPathway
  2. activation of cysteine-type endopeptidase activity involved in apoptotic process Source: FlyBase
  3. deoxyribonucleotide biosynthetic process Source: UniProtKB
  4. tissue regeneration Source: FlyBase
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

DNA replication

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

UniPathwayiUPA00326.

Names & Taxonomyi

Protein namesi
Recommended name:
Ribonucleoside-diphosphate reductase large subunit (EC:1.17.4.1)
Alternative name(s):
Ribonucleoside-diphosphate reductase subunit M1
Ribonucleotide reductase large subunit
Gene namesi
Name:RnrL
ORF Names:CG5371
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
ProteomesiUP000000803: Chromosome 2L

Organism-specific databases

FlyBaseiFBgn0011703. RnrL.

Subcellular locationi

GO - Cellular componenti

  1. ribonucleoside-diphosphate reductase complex Source: InterPro
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 812812Ribonucleoside-diphosphate reductase large subunit
PRO_0000187193Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi229 ↔ 455Redox-active By similarity
Modified residuei778 – 7781Phosphothreonine1 Publication
Modified residuei782 – 7821Phosphoserine1 Publication
Modified residuei786 – 7861Phosphotyrosine1 Publication

Keywords - PTMi

Disulfide bond, Phosphoprotein

Proteomic databases

PaxDbiP48591.

Expressioni

Gene expression databases

BgeeiP48591.

Interactioni

Subunit structurei

Heterodimer of a large and a small subunit.

Protein-protein interaction databases

BioGridi60477. 3 interactions.
DIPiDIP-19582N.
MINTiMINT-829510.

Structurei

3D structure databases

ProteinModelPortaliP48591.
SMRiP48591. Positions 26-753.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini12 – 10392ATP-cone
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni22 – 287Allosteric activator binding By similarity
Regioni228 – 2292Substrate binding By similarity
Regioni296 – 2994Allosteric effector binding, determines substrate specificity By similarity
Regioni438 – 4425Substrate binding By similarity
Regioni614 – 6185Substrate binding By similarity

Sequence similaritiesi

Contains 1 ATP-cone domain.

Phylogenomic databases

eggNOGiCOG0209.
GeneTreeiENSGT00390000001372.
InParanoidiP48591.
KOiK10807.
OMAiEACLMCQ.
OrthoDBiEOG7BGHK2.
PhylomeDBiP48591.

Family and domain databases

InterProiIPR005144. ATP-cone.
IPR013346. NrdE_NrdA.
IPR000788. RNR_lg_C.
IPR013509. RNR_lsu_N.
IPR008926. RNR_R1-su_N.
[Graphical view]
PfamiPF03477. ATP-cone. 1 hit.
PF02867. Ribonuc_red_lgC. 1 hit.
PF00317. Ribonuc_red_lgN. 1 hit.
[Graphical view]
PRINTSiPR01183. RIBORDTASEM1.
SUPFAMiSSF48168. SSF48168. 1 hit.
TIGRFAMsiTIGR02506. NrdE_NrdA. 1 hit.
PROSITEiPS51161. ATP_CONE. 1 hit.
PS00089. RIBORED_LARGE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P48591-1 [UniParc]FASTAAdd to Basket

« Hide

MLKNKSMKTS KLYVIKRDGR QEEVHFDKIT SRIQKLCYNL NMDFVDPVTI    50
TLQVINGLYC GVTTQELDNL AAEIAAGLTC NHPDYAILAA RIAVSNLHKE 100
TKKAFSDVFE DLYNHVNKET NQKVPLVSEF HYNVVKKNAT RLNSSIIYDR 150
DFGYNYFGFK TLERSYLLKR NGKIAERPQH MLMRVAIGIH GEDIDAAVET 200
YNLLSERYFT HASPTLFAAA TNRPQLSSCF LLTMTADSIE GIFKSVEQCA 250
MISKSAGGIG LNVHCIRAKG TSICGTNGTS NGLVPMLRVF NNVARYVDQG 300
GGKRPGAFAI YLEPWHSDVF EFLELKKNTG KEENRARDLF YALWIPDLFM 350
KRVEANGDWS LMCPHKCPGL HDVWGDEFEK LYEKYEQEGR ANRTVKAQSL 400
WFAIIEAQVE TGNPYMLFKD ACNRKSNQQN VGTIKCSNLC TEIVEYSAPD 450
EIAVCNLASI ALNMFVTPEK TYDFKKLKEV TKIVTKNLNK IIDINYYPLP 500
EARKSNLRHR PVGIGIQGFA DALILMRFPY ESEEAGLLNQ QIFETIYYGA 550
LEASCELAQT EGPYETYEGS PVSKGILQYD MWDKVPTNLW DWQKLKESIR 600
MHGVRNSLLV APMPTASTAQ IMGNNESFEP YTTNIYTRRV LSGEFQVVNH 650
HLLRDLTELD LWDDDMKNQI ISSRGSIQNI ETIPPKVRDL YKTVWEISVK 700
STIKMAADRG AFIDQSQSFN IHVAEPNYGK LTSIHFYSWK AGLKTGMYYL 750
RTKPAANAIQ FTVNKKQGAV SMNGQNGTAE GSPQKYEEDR ERKMADMVCS 800
LENKDACMSC GS 812
Length:812
Mass (Da):91,978
Last modified:December 1, 2000 - v2
Checksum:i6E4FC608AC04A5FD
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE014134 Genomic DNA. Translation: AAF52913.2.
AF132143 mRNA. Translation: AAD33590.1.
AY119149 mRNA. Translation: AAM51009.1.
U09369 Genomic DNA. Translation: AAA56995.1.
RefSeqiNP_477027.1. NM_057679.5.
UniGeneiDm.3216.

Genome annotation databases

EnsemblMetazoaiFBtr0080059; FBpp0079648; FBgn0011703.
GeneIDi34392.
KEGGidme:Dmel_CG5371.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE014134 Genomic DNA. Translation: AAF52913.2 .
AF132143 mRNA. Translation: AAD33590.1 .
AY119149 mRNA. Translation: AAM51009.1 .
U09369 Genomic DNA. Translation: AAA56995.1 .
RefSeqi NP_477027.1. NM_057679.5.
UniGenei Dm.3216.

3D structure databases

ProteinModelPortali P48591.
SMRi P48591. Positions 26-753.
ModBasei Search...

Protein-protein interaction databases

BioGridi 60477. 3 interactions.
DIPi DIP-19582N.
MINTi MINT-829510.

Proteomic databases

PaxDbi P48591.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblMetazoai FBtr0080059 ; FBpp0079648 ; FBgn0011703 .
GeneIDi 34392.
KEGGi dme:Dmel_CG5371.

Organism-specific databases

CTDi 34392.
FlyBasei FBgn0011703. RnrL.

Phylogenomic databases

eggNOGi COG0209.
GeneTreei ENSGT00390000001372.
InParanoidi P48591.
KOi K10807.
OMAi EACLMCQ.
OrthoDBi EOG7BGHK2.
PhylomeDBi P48591.

Enzyme and pathway databases

UniPathwayi UPA00326 .

Miscellaneous databases

GenomeRNAii 34392.
NextBioi 788275.
PROi P48591.

Gene expression databases

Bgeei P48591.

Family and domain databases

InterProi IPR005144. ATP-cone.
IPR013346. NrdE_NrdA.
IPR000788. RNR_lg_C.
IPR013509. RNR_lsu_N.
IPR008926. RNR_R1-su_N.
[Graphical view ]
Pfami PF03477. ATP-cone. 1 hit.
PF02867. Ribonuc_red_lgC. 1 hit.
PF00317. Ribonuc_red_lgN. 1 hit.
[Graphical view ]
PRINTSi PR01183. RIBORDTASEM1.
SUPFAMi SSF48168. SSF48168. 1 hit.
TIGRFAMsi TIGR02506. NrdE_NrdA. 1 hit.
PROSITEi PS51161. ATP_CONE. 1 hit.
PS00089. RIBORED_LARGE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "The genome sequence of Drosophila melanogaster."
    Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D.
    , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
    Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Berkeley.
  2. Cited for: GENOME REANNOTATION.
    Strain: Berkeley.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Berkeley.
    Tissue: Embryo.
  4. "Developmental control of a G1-S transcriptional program in Drosophila."
    Duronio R.J., O'Farrell P.H.
    Development 120:1503-1515(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 164-343.
    Strain: Oregon-R.
  5. "Phosphoproteome analysis of Drosophila melanogaster embryos."
    Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.
    J. Proteome Res. 7:1675-1682(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-778; SER-782 AND TYR-786, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Embryo.

Entry informationi

Entry nameiRIR1_DROME
AccessioniPrimary (citable) accession number: P48591
Secondary accession number(s): Q9UB08, Q9VKZ3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: December 1, 2000
Last modified: July 9, 2014
This is version 117 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

Allosteric enzyme, Complete proteome, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi